NMR study of macro domains (MDs) from betacoronavirus: backbone resonance assignments of SARS–CoV and MERS–CoV MDs in the free and the ADPr-bound state
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
https://link.springer.com/content/pdf/10.1007/s12104-021-10052-5.pdf
Reference27 articles.
1. Abraham R, Hauer D, McPherson RL et al (2018) ADP-ribosyl-binding and hydrolase activities of the alphavirus nsP3 macrodomain are critical for initiation of virus replication. Proc Natl Acad Sci USA 115(44):E10457–E10466. https://doi.org/10.1073/pnas.1812130115
2. Cantini F, Banci L, Altincekic N et al (2020) 1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS–CoV–2 non-structural protein 3b. Biomol NMR Assign 14:339–346. https://doi.org/10.1007/s12104-020-09973-4
3. Cho CC, Lin MH, Chuang CY, Hsu CH (2016) Macro domain from middle east respiratory syndrome coronavirus (MERS-CoV) is an efficient ADP-ribose binding module: crystal structure and biochemical studies. J Biol Chem 291(10):4894–4902. https://doi.org/10.1074/jbc.M115.700542
4. Fehr AR, Channappanavar R, Jankevicius G et al (2016) The conserved coronavirus macrodomain promotes virulence and suppresses the innate immune response during severe acute respiratory syndrome coronavirus. Infection. mBio 7(6):e01721-16. https://doi.org/10.1128/mBio.01721-16
5. Fehr AR, Jankevicius G, Ahel I, Perlman S (2018) Viral macrodomains: unique mediators of viral replication and pathogenesis. Trends Microbiol 26(7):598–610. https://doi.org/10.1016/j.tim.2017.11.011
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